Sortase‐Catalyzed Protein Domain Inversion
Abstract: Topological transformations and permutations of proteins have attracted significant interest as strategies to generate new protein functionalities or stability. These efforts have mainly been inspired by naturally occurring post‐translational modifications, such as head‐to‐tail cyclization, circular permutation, or lasso‐like entanglement. Such approaches can be realized experimentally via genetic encoding, in the case of circular permutation, or via enzymatic processing, in the case of cyclization. Notably, these previously described strategies leave the polypeptide backbone orientation unaltered. Here we describe an unnatural protein permutation, the protein domain inversion, whereby a C‐terminal portion of a protein is enzymatically inverted from the canonical N‐to‐C to a C‐to‐C configuration with respect to the N‐terminal part of the protein. The closest conceptually analogous biological process is perhaps the inversion of DNA segments as catalyzed by recombinases. We achieve these inversions using an engineered sortase A, a widely used transpeptidase. Our reactions proceed efficiently under mild conditions at 4–25 °C and are compatible with entirely heterologously‐produced protein substrates.
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Erschienen in
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Sortase‐Catalyzed Protein Domain Inversion ; day:29 ; month:02 ; year:2024 ; extent:8
Angewandte Chemie ; (29.02.2024) (gesamt 8)
- Urheber
- DOI
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10.1002/ange.202316777
- URN
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urn:nbn:de:101:1-2024030114021671893761
- Rechteinformation
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
- 14.08.2025, 10:49 MESZ
Datenpartner
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Zhou, Yan
- Durek, Thomas
- Craik, David
- Rehm, Fabian B. H.
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